alpha-chymotrypsin and phevalin

Overexpression of a putative type III polyketide synthase (PKSIII) from the marine myxobacterium Enhygromyxa salina SWB007 in Streptoinyces coelicolor MI 146 led to the accumulation of a novel monoketopiperazine consisting of phenylalanine and isoleucine. This compound was named phileucin and shows high structural similarity to phevalin (aureusimine B). The protease inhibiting activity was tested against human cathepsin L, human leukocyte elastase; bovine trypsin and bovine chymotrypsin. In contrast to phevalin, no protease inhibition was observed.

Topics: Animals; Cathepsin L; Cattle; Chymotrypsin; Humans; Magnetic Resonance Spectroscopy; Myxococcales; Polyketide Synthases; Protease Inhibitors; Proteinase Inhibitory Proteins, Secretory; Pyrazines; Spectrometry, Mass, Electrospray Ionization; Spectrophotometry, Infrared; Spectrophotometry, Ultraviolet; Streptomyces coelicolor; Trypsin Inhibitors